TRI34_HUMAN
ID TRI34_HUMAN Reviewed; 488 AA.
AC Q9BYJ4; D3DQS7; Q9C016; Q9HCR0; Q9HCR1; Q9HCR2;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Tripartite motif-containing protein 34;
DE AltName: Full=Interferon-responsive finger protein 1;
DE AltName: Full=RING finger protein 21;
GN Name=TRIM34; Synonyms=IFP1, RNF21;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING,
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=11013086; DOI=10.1006/geno.2000.6318;
RA Orimo A., Tominaga N., Yoshimura K., Yamauchi Y., Nomura M., Sato M.,
RA Nogi Y., Suzuki M., Suzuki H., Ikeda K., Inoue S., Muramatsu M.;
RT "Molecular cloning of ring finger protein 21 (RNF21)/interferon-responsive
RT finger protein (ifp1), which possesses two RING-B box-coiled coil domains
RT in tandem.";
RL Genomics 69:143-149(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thyroid;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-488 (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, INTERACTION WITH TRIM5, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=17156811; DOI=10.1016/j.virol.2006.10.035;
RA Li X., Gold B., O'hUigin C., Diaz-Griffero F., Song B., Si Z., Li Y.,
RA Yuan W., Stremlau M., Mische C., Javanbakht H., Scally M., Winkler C.,
RA Dean M., Sodroski J.;
RT "Unique features of TRIM5alpha among closely related human TRIM family
RT members.";
RL Virology 360:419-433(2007).
RN [7]
RP INTERACTION WITH TRIM5, AND MUTAGENESIS OF ARG-121.
RX PubMed=21680743; DOI=10.1074/jbc.m111.260406;
RA Li X., Yeung D.F., Fiegen A.M., Sodroski J.;
RT "Determinants of the higher order association of the restriction factor
RT TRIM5alpha and other tripartite motif (TRIM) proteins.";
RL J. Biol. Chem. 286:27959-27970(2011).
RN [8]
RP STRUCTURE BY NMR OF 8-79.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RING-finger domain from human tripartite motif
RT protein 34.";
RL Submitted (SEP-2007) to the PDB data bank.
CC -!- FUNCTION: May function as antiviral protein and may contribute to the
CC defense against retroviral infections. {ECO:0000269|PubMed:17156811}.
CC -!- SUBUNIT: Homotrimer. Interacts (via the B30.2/SPRY domain) with HIV-1
CC capsid complexes (PubMed:17156811). Interacts (via B-box and SPRY
CC domain) with TRIM5 (PubMed:21680743, PubMed:17156811).
CC {ECO:0000269|PubMed:17156811, ECO:0000269|PubMed:21680743}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17156811}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Medium;
CC IsoId=Q9BYJ4-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q9BYJ4-2; Sequence=VSP_011921, VSP_011922;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Is the most abundant form. It is
CC highly expressed in the placenta, spleen, colon and peripheral blood
CC leukocytes. {ECO:0000269|PubMed:11013086}.
CC -!- INDUCTION: [Isoform 1]: Up-regulated by interferons.
CC {ECO:0000269|PubMed:11013086}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG53517.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB17050.1; Type=Miscellaneous discrepancy; Note=The in vivo relevance of this transcript of the TRIM6 (AC Q9C030) and TRIM34 genes creating a chimeric protein of 842 residues is uncertain.; Evidence={ECO:0000305};
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DR EMBL; AB039902; BAB17049.1; -; mRNA.
DR EMBL; AB039903; BAB17050.1; ALT_SEQ; mRNA.
DR EMBL; AB039904; BAB17051.1; -; mRNA.
DR EMBL; AF220143; AAG53516.1; -; mRNA.
DR EMBL; AF220144; AAG53517.1; ALT_INIT; mRNA.
DR EMBL; AK027876; BAB55424.1; -; mRNA.
DR EMBL; CH471064; EAW68778.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68780.1; -; Genomic_DNA.
DR EMBL; AL583914; CAC29498.1; -; mRNA.
DR CCDS; CCDS31391.1; -. [Q9BYJ4-1]
DR RefSeq; NP_001003827.1; NM_001003827.1. [Q9BYJ4-1]
DR RefSeq; NP_067629.2; NM_021616.5. [Q9BYJ4-1]
DR RefSeq; NP_569074.2; NM_130390.2.
DR PDB; 2EGP; NMR; -; A=8-79.
DR PDBsum; 2EGP; -.
DR AlphaFoldDB; Q9BYJ4; -.
DR SMR; Q9BYJ4; -.
DR BioGRID; 119809; 17.
DR IntAct; Q9BYJ4; 6.
DR STRING; 9606.ENSP00000346916; -.
DR iPTMnet; Q9BYJ4; -.
DR PhosphoSitePlus; Q9BYJ4; -.
DR BioMuta; TRIM34; -.
DR DMDM; 55976584; -.
DR EPD; Q9BYJ4; -.
DR jPOST; Q9BYJ4; -.
DR MassIVE; Q9BYJ4; -.
DR MaxQB; Q9BYJ4; -.
DR PaxDb; Q9BYJ4; -.
DR PeptideAtlas; Q9BYJ4; -.
DR PRIDE; Q9BYJ4; -.
DR ProteomicsDB; 79657; -. [Q9BYJ4-1]
DR ProteomicsDB; 79658; -. [Q9BYJ4-2]
DR Antibodypedia; 57793; 141 antibodies from 19 providers.
DR DNASU; 53840; -.
DR Ensembl; ENST00000429814.3; ENSP00000402595.2; ENSG00000258659.7. [Q9BYJ4-1]
DR Ensembl; ENST00000514226.5; ENSP00000422947.1; ENSG00000258659.7. [Q9BYJ4-1]
DR GeneID; 53840; -.
DR KEGG; hsa:53840; -.
DR MANE-Select; ENST00000429814.3; ENSP00000402595.2; NM_021616.6; NP_067629.2.
DR UCSC; uc001mbh.4; human. [Q9BYJ4-1]
DR CTD; 53840; -.
DR DisGeNET; 53840; -.
DR GeneCards; TRIM34; -.
DR HGNC; HGNC:10063; TRIM34.
DR HPA; ENSG00000258659; Low tissue specificity.
DR MIM; 605684; gene.
DR neXtProt; NX_Q9BYJ4; -.
DR OpenTargets; ENSG00000258659; -.
DR PharmGKB; PA35533; -.
DR VEuPathDB; HostDB:ENSG00000258659; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000162320; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q9BYJ4; -.
DR OMA; PMILCPP; -.
DR OrthoDB; 165920at2759; -.
DR PhylomeDB; Q9BYJ4; -.
DR PathwayCommons; Q9BYJ4; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q9BYJ4; -.
DR BioGRID-ORCS; 53840; 10 hits in 1055 CRISPR screens.
DR EvolutionaryTrace; Q9BYJ4; -.
DR GenomeRNAi; 53840; -.
DR Pharos; Q9BYJ4; Tbio.
DR PRO; PR:Q9BYJ4; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9BYJ4; protein.
DR Bgee; ENSG00000258659; Expressed in monocyte and 101 other tissues.
DR Genevisible; Q9BYJ4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0032880; P:regulation of protein localization; IBA:GO_Central.
DR GO; GO:0046596; P:regulation of viral entry into host cell; IBA:GO_Central.
DR CDD; cd15825; SPRY_PRY_TRIM34; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035826; TRIM34_PRY/SPRY.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense; Coiled coil;
KW Cytoplasm; Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..488
FT /note="Tripartite motif-containing protein 34"
FT /id="PRO_0000056248"
FT DOMAIN 283..488
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 15..60
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 92..134
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 131..239
FT /evidence="ECO:0000255"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 259..270
FT /note="SEIWRLKKPKMV -> CVWVATSGACEL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11013086"
FT /id="VSP_011921"
FT VAR_SEQ 271..488
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11013086"
FT /id="VSP_011922"
FT VARIANT 276
FT /note="T -> S (in dbSNP:rs6578670)"
FT /id="VAR_019825"
FT VARIANT 282
FT /note="D -> H (in dbSNP:rs3740997)"
FT /id="VAR_019826"
FT VARIANT 404
FT /note="N -> K (in dbSNP:rs16933844)"
FT /id="VAR_052141"
FT MUTAGEN 121
FT /note="R->E: Reduced association with TRIM5."
FT /evidence="ECO:0000269|PubMed:21680743"
FT CONFLICT 349
FT /note="H -> Y (in Ref. 5)"
FT /evidence="ECO:0000305"
FT TURN 16..19
FT /evidence="ECO:0007829|PDB:2EGP"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2EGP"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:2EGP"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2EGP"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2EGP"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2EGP"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2EGP"
SQ SEQUENCE 488 AA; 56864 MW; F2D60A16576187A0 CRC64;
MASKILLNVQ EEVTCPICLE LLTEPLSLDC GHSLCRACIT VSNKEAVTSM GGKSSCPVCG
ISYSFEHLQA NQHLANIVER LKEVKLSPDN GKKRDLCDHH GEKLLLFCKE DRKVICWLCE
RSQEHRGHHT VLTEEVFKEC QEKLQAVLKR LKKEEEEAEK LEADIREEKT SWKYQVQTER
QRIQTEFDQL RSILNNEEQR ELQRLEEEEK KTLDKFAEAE DELVQQKQLV RELISDVECR
SQWSTMELLQ DMSGIMKWSE IWRLKKPKMV SKKLKTVFHA PDLSRMLQMF RELTAVRCYW
VDVTLNSVNL NLNLVLSEDQ RQVISVPIWP FQCYNYGVLG SQYFSSGKHY WEVDVSKKTA
WILGVYCRTY SRHMKYVVRR CANRQNLYTK YRPLFGYWVI GLQNKCKYGV FEESLSSDPE
VLTLSMAVPP CRVGVFLDYE AGIVSFFNVT SHGSLIYKFS KCCFSQPVYP YFNPWNCPAP
MTLCPPSS
